The open-air site of Tolbor 16 (Northern Mongolia): Preliminary results and perspectives.

Numerous questions remain regarding the timing and the context of Upper Paleolithic emergence in Northeast Asia. Available data allow the recognition of a form of Initial Upper Paleolithic (IUP) documented in the Altai circa 45e40 ka 14C BP, and in the Cis- and Transbaikal around �37 ka 14C BP. In Northern Mongolia, a series of assemblages show intriguing similarities with IUP laminar assemblages from South Siberia and suggest long distance contact/movements of population during the first half of MIS3. These contacts are potentially enabled by the main river that drains into Lake Baikal, the Selenga. By cutting through the Sayan and the Yablonovy mountain ranges, the Selenga drainage system provides a potential corridor connecting South Siberia with the plains of Mongolia. The Tolbor 16 site (Ikh Tulberiin Gol, Northern Mongolia) is located circa 13 km from the confluence with the Selenga. The first results presented here suggest that the lithic assemblage and the ornaments discovered at Tolbor 16 document the early appearance of Upper Paleolithic in the region. This newly discovered site offers the possibility to generate high-resolution contextual data on the first appearance of the blade assemblages in Mongolia and to test the ‘Selenga corridor hypothesis’

Coordination of selenium to molybdenum in formate dehydrogenase H from \u3ci\u3eEscherichia coli\u3c/i\u3e

Formate dehydrogenase H from Escherichia col contains multiple redox centers, which include a molybdopterin cofactor, an iron-sulfur center, and a selenocysteine residue (SeCys-140 in the polypeptide chain) that is essential for catalytic activity. Here we show that addition of formate to the native enzyme induces a signal typical of Mo(V) species. This signal is detected by electron pm etc resonance (EPR) spectroscopy. Substitution of 77Se for natural isotope abundance Se leads to transformation of this signal, indicating a direct coordination of Se with Mo. Mutant enzyme with cysteine substituted at position 140 for the selenocysteine residue has decreased catalytic activity and exhibits a different EPR signal. Since deternation of the Se content of wild-type enzyme indicates 1 gram atom per mol, we conclude that it is the Se atom of the SeCys-140 residue in the protein that is coordinated directly with Mo. The amino acd sequence flanking the selenocysteine residue in formate dehydrogenase H is s r to a conserved sequence found in several other prokaryotic molybdopterin-dependent enzymes. In most of these other enzymes a cysteine residue, or in a few cases a serine or a selenocysteine residue, occurs in the position corresonding to SeCys-140 of formate dehydrogeme H. By analogy with formate dehydrogenase H in these other enzymes, at least one of the ilgands to Mo should be provided by an amino acid residue of the protein. This igand could be the Se of a selenocysteine residue, sulfur of a cysteine residue, or, in the case of a serine residue, oxygen